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Database: UniProt
Entry: A0A2Y9NHB9_DELLE
LinkDB: A0A2Y9NHB9_DELLE
Original site: A0A2Y9NHB9_DELLE 
ID   A0A2Y9NHB9_DELLE        Unreviewed;       863 AA.
AC   A0A2Y9NHB9;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=dynamin GTPase {ECO:0000256|ARBA:ARBA00011980};
DE            EC=3.6.5.5 {ECO:0000256|ARBA:ARBA00011980};
GN   Name=DNM1 {ECO:0000313|RefSeq:XP_022434329.1};
OS   Delphinapterus leucas (Beluga whale).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Monodontidae; Delphinapterus.
OX   NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022434329.1};
RN   [1] {ECO:0000313|RefSeq:XP_022434329.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022434329.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC       superfamily. Dynamin/Fzo/YdjA family. {ECO:0000256|RuleBase:RU003932}.
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DR   RefSeq; XP_022434329.1; XM_022578621.2.
DR   AlphaFoldDB; A0A2Y9NHB9; -.
DR   Proteomes; UP000248483; Unplaced.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   CDD; cd08771; DLP_1; 1.
DR   CDD; cd01256; PH_dynamin; 1.
DR   Gene3D; 1.20.120.1240; Dynamin, middle domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR022812; Dynamin.
DR   InterPro; IPR001401; Dynamin_GTPase.
DR   InterPro; IPR019762; Dynamin_GTPase_CS.
DR   InterPro; IPR045063; Dynamin_N.
DR   InterPro; IPR000375; Dynamin_stalk.
DR   InterPro; IPR030381; G_DYNAMIN_dom.
DR   InterPro; IPR003130; GED.
DR   InterPro; IPR020850; GED_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR11566; DYNAMIN; 1.
DR   PANTHER; PTHR11566:SF32; DYNAMIN-1; 1.
DR   Pfam; PF01031; Dynamin_M; 1.
DR   Pfam; PF00350; Dynamin_N; 1.
DR   Pfam; PF02212; GED; 1.
DR   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00195; DYNAMIN.
DR   SMART; SM00053; DYNc; 1.
DR   SMART; SM00302; GED; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS00410; G_DYNAMIN_1; 1.
DR   PROSITE; PS51718; G_DYNAMIN_2; 1.
DR   PROSITE; PS51388; GED; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   3: Inferred from homology;
KW   Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU003932};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003932};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248483}.
FT   DOMAIN          28..294
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   DOMAIN          515..621
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          655..746
FT                   /note="GED"
FT                   /evidence="ECO:0000259|PROSITE:PS51388"
FT   REGION          763..863
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        763..777
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        778..854
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   863 AA;  96989 MW;  E4D961E0D775537E CRC64;
     MGNRGMEDLI PLVNRLQDAF SAIGQNADLD LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG
     SGIVTRRPLV LQLVNATTEY AEFLHCKGKK FTDFEEVRLE IEAETDRVTG TNKGISPVPI
     NLRVYSPHVL NLTLVDLPGM TKVPVGDQPP DIEFQIRDML MQFVTKENCL ILAVSPANSD
     LANSDALKVA KEVDPQGQRT IGVITKLDLM DEGTDARDVL ENKLLPLRRG YIGVVNRSQK
     DIDGKKDITA ALAAERKFFL SHPSYRHLAD RMGTPYLQKV LNQQLTNHIR DTLPGLRNKL
     QSQLLSIEKE VEEYKNFRPD DPARKTKALL QMVQQFAVDF EKRIEGSGDQ IDTYELSGGA
     RINRIFHERF PFELVKMEFD EKELRREISY AIKNIHGIRT GLFTPDLAFE ATVKKQVQKL
     KEPSIKCVDM VVSELTATIR KCSEKLQQYP RLREEMERIV TTHIREREGR TKEQVMLLID
     IELAYMNTNH EDFIGFANAQ QRSNQMNKKK ASGNQVIRKG WLTINNIGIM KGGSKEYWFV
     LTAENLSWYK DDEEKEKKYM LSVDNLKLRD VEKGFMSSKH VFALFNTEQR NVYKDYRQLE
     LACETQEEVD SWKASFLRAG VYPERVGDKE KASETEENGS DNFMHSMDPQ LERQVETIRN
     LVDSYMAIVN KTVRDLMPKT IMHLMINNTK EFIFSELLAN LYSCGDQNTL MEESAEQAQR
     RDEMLRMYHA LKEALSIIGD INTTTVSTPM PPPVDDSWLQ VQSVPAGRRS PTSSPTPQRR
     APAVPPARPG SRGPAPGPPP AGSALGGAPP VPSRPGASPD PFGPPPQVPS RPNRAPPGVP
     RKGPASPTRP AAPRPAEAPL LDL
//
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